ID   PEPT_BACC3              Reviewed;         410 AA.
AC   C1ENW4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Peptidase T {ECO:0000255|HAMAP-Rule:MF_00550};
DE            EC=3.4.11.4 {ECO:0000255|HAMAP-Rule:MF_00550};
DE   AltName: Full=Aminotripeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
DE            Short=Tripeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
DE   AltName: Full=Tripeptide aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
GN   Name=pepT {ECO:0000255|HAMAP-Rule:MF_00550}; OrderedLocusNames=BCA_3837;
OS   Bacillus cereus (strain 03BB102).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=572264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03BB102;
RA   Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C.,
RA   Tapia R., Han C., Sutton G., Sims D.;
RT   "Genome sequence of Bacillus cereus 03BB102.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides.
CC       {ECO:0000255|HAMAP-Rule:MF_00550}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of the N-terminal residue from a tripeptide.;
CC         EC=3.4.11.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00550};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00550};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00550};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00550}.
CC   -!- SIMILARITY: Belongs to the peptidase M20B family. {ECO:0000255|HAMAP-
CC       Rule:MF_00550}.
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DR   EMBL; CP001407; ACO29109.1; -; Genomic_DNA.
DR   RefSeq; WP_000656979.1; NZ_CP009318.1.
DR   AlphaFoldDB; C1ENW4; -.
DR   SMR; C1ENW4; -.
DR   MEROPS; M20.003; -.
DR   EnsemblBacteria; ACO29109; ACO29109; BCA_3837.
DR   KEGG; bcx:BCA_3837; -.
DR   PATRIC; fig|572264.18.peg.3794; -.
DR   OMA; GHNFHGK; -.
DR   Proteomes; UP000002210; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00550; Aminopeptidase_M20; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR010161; Peptidase_M20B.
DR   PANTHER; PTHR42994:SF1; PTHR42994:SF1; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037215; Peptidase_M20B; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01882; peptidase-T; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Zinc.
FT   CHAIN           1..410
FT                   /note="Peptidase T"
FT                   /id="PRO_1000200883"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         199
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         381
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
SQ   SEQUENCE   410 AA;  45867 MW;  6B489FDF6B33539D CRC64;
     MKEELIERFT RYVKIDTQSN EDSHTVPTTP GQIEFGKLLV EELKEVGLTE VTMDDNGYVM
     ATLPANTDKD VPVIGFLAHL DTATDFTGKN VKPQIHENFD GNAITLNEEL NVVLTPEQFP
     ELPSYKGHTI ITTDGTTLLG ADDKAGLTEI MVAMNYLIHN PQIKHGKIRV AFTPDEEIGR
     GPAHFDVEAF GASFAYTMDG GPLGGLEYES FNAAGAKLTF NGTNTHPGTA KNKMRNATKL
     AMEFNGHLPV EEAPEYTEGY EGFYHLLSLN GDVEQSKAYY IIRDFDRKNF EARKNTIENI
     VKQMQEKYGQ DAVVLEMNDQ YYNMLEKIEP VREIVDIAYE AMKSLNIEPN IHPIRGGTDG
     SQLSYMGLPT PNIFTGGENY HGKFEYVSVD VMEKAVQVII EIARRFEEQA